Capillary electrophoresis analysis of the degradation of the aspartyl tripeptide Phe-Asp-GlyOH at pH 2.0 and 7.4 under forced conditions

Journal of Pharmaceutical and Biomedical Analysis

Volumn 51, Issue 3, 2010, Pages 640-648

  Conrad, Uwe ^a   Taichrib, Angelina ^b   Neusüß, Christian ^b   Scriba, Gerhard K E ^a  

^a FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

^b AALEN UNIVERSITY   (Germany)

Author keywords

Aspartyl peptide; Capillary electrophoresis; Enantiomerization; Isomerization; Kinetics; Peptide degradation

Indexed keywords

ACETONITRILE; ASPARTYL TRIPEPTIDE; CARBOXYMETHYL BETA CYCLODEXTRIN; ELECTROLYTE; PHENYLALANYL ALPHA ASPARTYLGLYCINE HYDROXIDE; PHENYLALANYL ALPHA DEXTRO ASPARTYLGLYCINE HYDROXIDE; PHENYLALANYLASPARTYLGLYCINE HYDROXIDE; PIPERAZINEDIONE; SODIUM DIHYDROGEN PHOSPHATE; TRIPEPTIDE; UNCLASSIFIED DRUG;

ACCURACY; ARTICLE; CAPILLARY ELECTROPHORESIS; CONTROLLED STUDY; DIASTEREOISOMER; ELECTROSPRAY MASS SPECTROMETRY; EPIMERIZATION; INCUBATION TIME; ISOMERIZATION; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN HYDROLYSIS; SENSITIVITY AND SPECIFICITY; TEMPERATURE;

ASPARTIC ACID; ELECTROPHORESIS, CAPILLARY; GLYCINE; HYDROGEN-ION CONCENTRATION; HYDROXIDES; PEPTIDES; PHENYLALANINE;

EID: 70350605474     PISSN: 07317085     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jpba.2009.09.044     Document Type: Article

References (33)

1. Manning M.C., Patel K., and Borchardt R.T. Stability of protein pharmaceuticals. Pharm. Res. 6 (1989) 903-918
2. Aswad D.W. Deamidation and Isoaspartate Formation in Peptides and Proteins (1995), CRC Press, Boca Raton
3. Stephenson R.C., and Clarke S. Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J. Biol. Chem. 264 (1989) 6164-6170
4. Geiger T., and Clarke S. Deamidation, isomierization, and racemization at asparaginyl and aspartyl residues in peptides. J. Biol. Chem. 262 (1987) 785-794
5. Oliyai C., and Borchardt R.T. Chemical pathways of peptide degradation. VI. Effect of the primary sequence on the pathways of degradation of aspartyl residues in model hexapeptides. Pharm. Res. 11 (1994) 751-758
6. Won C.M., Molnar T.E., Windisch V.L., and McKean R.E. Kinetics and mechanism of degradation of klerval, a pseudo-tetrapeptide. Int. J. Pharm. 190 (1999) 1-11
7. De Boni S., and Scriba G.K.E. Capillary electrophoresis analysis of hydrolysis, isomerization and enantiomerization of aspartyl model tripeptides in acidic and alkaline solution. J. Pharm. Biomed. Anal. 43 (2007) 49-56
8. Radkiewicz J.L., Zipse H., Clarke S., and Houk K.N. Accelerated racemization of aspartic acid and asparagine residues via succinimide intermediates: An ab initio theoretical exploration of mechanism. J. Am. Chem. Soc. 118 (1996) 9148-9155
9. Li B., Borchardt R.T., Topp E.M., VanderVelde D., and Schowen R.L. Racemization of an asparagine residue during peptide deamidation. J. Am. Chem. Soc. 125 (2003) 11486-11487
10. Oliyai C., and Borchardt R.T. Chemical pathways of peptide degradation. IV. Pathways, kinetics, and mechanism of degradation of an aspartyl residue in a model hexapeptide. Pharm. Res. 10 (1993) 95-102
11. Wakankar A.A., and Borchardt R.T. Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization. J. Pharm. Sci. 95 (2006) 2321-2336
12. Athmer L., Kindrachuk J., Georges F., and Napper S. The influence of protein structure on the products emerging from succinimide hydrolysis. J. Biol. Chem. 277 (2002) 30502-30507
13. Steinberg S.M., Masters P.M., and Bada J.L. The racemization of free and peptide-bound serine and aspartic acid at 100̊C as a function of pH: Implications for in vivo racemization. Bioorg. Chem. 12 (1984) 349-355
14. Ritz-Timme S., and Collins M.J. Racemization of aspartic acid in human proteins. Ageing Res. Rev. 1 (2002) 43-59
15. Fisher G.H., Payan I.L., Chou S.J., Man E.H., Cerwinski S., Martin T., Emory C., and Frey W.H. Racemized D-aspartate in Alzheimer neurofibrillary tangles. Brain Res. Bull. 28 (1992) 127-131
16. Orpiszewski J., Schormann N., Kluve-Beckerman B., Liepnieks J.J., and Benson M.D. Protein aging hypothesis of Alzheimer disease. FASEB J. 14 (2000) 1255-1263
17. Hekman C.M., DeMond W.S., Kelley P.J., Mauch S.F., and Williams J.D. Isolation and identification of cyclic imide and deamidation products in heat stressed pramlintide injection drug product. J. Pharm. Biomed. Anal. 20 (1999) 763-772
18. Weiss M., Manneberg M., Juranville J.-F., Lahm H.-W., and Fountoulakis M. Effect of the hydrolysis method on the determination of the amino acid composition of proteins. J. Chromatogr. A 795 (1998) 263-275
19. Smith D.G., Stein W.H., and Moore S. The sequence of amino acid residues in bovine pancreatic ribonuclease: Revisions and confirmations. J. Biol. Chem. 238 (1963) 227-234
20. Kasicka V. Recent developments in capillary electrophoresis and capillary electrochromatography of peptides. Electrophoresis 27 (2006) 142-175
21. Kasicka V. Recent developments in CE and CEC of peptides. Electrophoresis 29 (2008) 179-206
22. Scriba G.K.E. Recent advances in peptide and peptidomimetic stereoisomer separation by capillary electromigration techniques. Electrophoresis 27 (2006) 222-230
23. Scriba G.K.E. Recent developments in peptide stereoisomer separations by capillary electromigration techniques. Electrophoresis 30 (2009) S222-S228
24. De Boni S., Neusüß C., Pelzing M., and Scriba G.K.E. Identification of degradation products of aspartyl tripeptides by capillary electrophoresis-tandem mass spectrometry. Electrophoresis 24 (2003) 874-882
25. De Boni S., Oberthür C., Hamburger M., and Scriba G.K.E. Analysis of aspartyl peptide degradation products by high-performance liquid chromatography and high-performance liquid chromatography-mass spectrometry. J. Chromatogr. A 1022 (2004) 95-102
26. DeHart M.P., and Anderson B.D. The role of the cyclic imide in alternate degradation pathways for asparagine-containing peptides and proteins. J. Pharm. Sci. 96 (2007) 2667-2685
27. Schön I., and Kisfaludy L. Formation of aminosuccinyl peptides during acidolytic deprotection followed by their transformation to piperazine-2,5-dione derivates in neutral media. Int. J. Peptide Protein Res. 14 (1979) 485-494
28. Roepstorff P., and Fohlman J. Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 11 (1984) 601
29. Biemann K. Nomenclature for peptide fragment ions (positive ions). Method Enzymol. 193 (1990) 886-887
30. Lehmann W.D., Schlosser A., Erben G., Pipkorn R., Bossemeyer D., and Kinzel V. Analysis of isoaspartate in peptides by electrospray tandem mass spectrometry. Protein Sci. 9 (2000) 2260-2268
31. Patel K., and Borchardt R.T. Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in a model hexapeptide. Pharm. Res. 7 (1990) 703-711
32. Cloos P.A.C., and Fidelius C. Collagen fragments in urine derived from bone resorption are highly racemized and isomerized: A biological clock of protein aging with clinical potential. Biochem. J. 345 (2000) 473-480
33. Kaneda M., Nakagomi K., Sadakane Y., Yamazaki T., Tanimura T., Akizawa T., Fujii N., and Hatanaka Y. A rapid HPLC determination of the isomerization level of Asp-residues within synthetic alpha-A-crystallin fragments. J. Liq. Chromatogr. Rel. Technol. 25 (2002) 2445-2454